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Conserved domains on  [gi|392928060|ref|NP_001257258|]
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protein KINase [Caenorhabditis elegans]

Protein Classification

STKc_CK1_delta_epsilon domain-containing protein (domain architecture ID 10197527)

STKc_CK1_delta_epsilon domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
8-281 0e+00

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271027  Cd Length: 275  Bit Score: 580.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGP 87
Cdd:cd14125    1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  88 SLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRGNLVYIIDFGLAKRYRDSK-HQHIAY 166
Cdd:cd14125   81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKYRDPRtHQHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 167 RENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKAVTKRQKYELISEKKISTRVDDLCAGYPEA 246
Cdd:cd14125  161 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPSE 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 392928060 247 FAQYLNYCRSLGFEEQPDYGYLRNLFRTLFHRQQF 281
Cdd:cd14125  241 FATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
 
Name Accession Description Interval E-value
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
8-281 0e+00

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027  Cd Length: 275  Bit Score: 580.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGP 87
Cdd:cd14125    1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  88 SLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRGNLVYIIDFGLAKRYRDSK-HQHIAY 166
Cdd:cd14125   81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKYRDPRtHQHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 167 RENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKAVTKRQKYELISEKKISTRVDDLCAGYPEA 246
Cdd:cd14125  161 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPSE 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 392928060 247 FAQYLNYCRSLGFEEQPDYGYLRNLFRTLFHRQQF 281
Cdd:cd14125  241 FATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
9-284 6.30e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 131.79  E-value: 6.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   9 FRLGRKIGSGSFGDIYLGQNIQTN--EEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELL- 85
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDRKLValKVLAKKLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVMEYVd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  86 GPSLEDLF--NFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNLVYIIDFGLAKRYRDSKHQH 163
Cdd:COG0515   82 GGSLEDLLkkIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIL--LDRDGRVVKLIDFGLAKLLPDPGSTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 164 IAYRENKNLTGTARYASINTHRGIEQ---SRRDDIESLGYVFMYFNRGTLPWQGLKAV-----TKRQKYELISEKKISTR 235
Cdd:COG0515  160 SIPALPSTSVGTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSsatsqTLKIILELPTPSLASPL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 392928060 236 VDDLCAGYPEAFAQYLNycRSLGFEEQPDYGYLRNLFRTLFHRQQFCYD 284
Cdd:COG0515  240 SPSNPELISKAASDLLK--KLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
9-239 3.78e-27

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567  Cd Length: 254  Bit Score: 107.62  E-value: 3.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060     9 FRLGRKIGSGSFGDIYLGQNIQTNEEVAVK---LECVKSKHPQLHIESRLYRiMLGGIGIPEIRWCGQEGDYNVMVMELL 85
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILK-KLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060    86 -GPSLEDLFNFcQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNlVYIIDFGLAKRYRDSKHQHi 164
Cdd:smart00220  80 eGGDLFDLLKK-RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL--LDEDGH-VKLADFGLARQLDPGEKLT- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   165 ayrenkNLTGTARYASINTHRGIEQSRRDDIESLGyVFMY-FNRGTLPWQG-------LKAVTKRQKYELISEKKISTRV 236
Cdd:smart00220 155 ------TFVGTPEYMAPEVLLGKGYGKAVDIWSLG-VILYeLLTGKPPFPGddqllelFKKIGKPKPPFPPPEWDISPEA 227

                   ...
gi 392928060   237 DDL 239
Cdd:smart00220 228 KDL 230
Pkinase pfam00069
Protein kinase domain;
9-214 2.47e-22

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 93.82  E-value: 2.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060    9 FRLGRKIGSGSFGDIYLGQNIQTNEEVAVKleCVKSKHPQLHIESRLYR---IM--LGGIGIPEIRWCGQEGDYNVMVME 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIK--KIKKEKIKKKKDKNILReikILkkLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   84 LL-GPSLEDLFNFcQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNLvYIIDFGLAKRYRDSKhq 162
Cdd:pfam00069  79 YVeGGSLFDLLSE-KGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENIL--IDEDGNL-KITDFGLARQLNSGS-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392928060  163 hiayrENKNLTGTARYAS--INTHRGIeqSRRDDIESLGYVFMYFNRGTLPWQG 214
Cdd:pfam00069 153 -----SLTSFVGTPWYMApeVLRGNPY--GPKVDVWSLGCILYELLTGKPPFPG 199
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
6-272 1.27e-21

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 92.32  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   6 GNRFRLGRKIGSGSFGDIYLGQ---NIQTNEEVAVKLECVKSKhpQLHIESRLYRIM--------------LGGIGIPEI 68
Cdd:PHA02882  11 GKEWKIDKLIGCGGFGCVYETQcasDHCINNQAVAKIENLENE--TIVMETLVYNNIydidkialwknihnIDHLGIPKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  69 RWCGQ----EGDYNVMVMELLGPSLEDLFN--FCQRKFSLKTVLLladQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRG 142
Cdd:PHA02882  89 YGCGSfkrcRMYYRFILLEKLVENTKEIFKriKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMVDGNNRG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 143 nlvYIIDFGLAKrYRDSKHQHIAY-RENKNL-TGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKA--- 217
Cdd:PHA02882 166 ---YIIDYGIAS-HFIIHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHngn 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392928060 218 ---VTKRQKYELISEKKISTRVDDlcagypEAFAQYLNYCRSLGFEEQPDYGYLRNLF 272
Cdd:PHA02882 242 lihAAKCDFIKRLHEGKIKIKNAN------KFIYDFIECVTKLSYEEKPDYDALIKIF 293
 
Name Accession Description Interval E-value
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
8-281 0e+00

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027  Cd Length: 275  Bit Score: 580.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGP 87
Cdd:cd14125    1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  88 SLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRGNLVYIIDFGLAKRYRDSK-HQHIAY 166
Cdd:cd14125   81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKYRDPRtHQHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 167 RENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKAVTKRQKYELISEKKISTRVDDLCAGYPEA 246
Cdd:cd14125  161 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPSE 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 392928060 247 FAQYLNYCRSLGFEEQPDYGYLRNLFRTLFHRQQF 281
Cdd:cd14125  241 FATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
8-272 0e+00

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918  Cd Length: 266  Bit Score: 503.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGP 87
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  88 SLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRGNLVYIIDFGLAKRYRDSK-HQHIAY 166
Cdd:cd14016   81 SLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLAKKYRDPRtGKHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 167 RENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKAVTKRQKYELISEKKISTRVDDLCAGYPEA 246
Cdd:cd14016  161 REGKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWQGLKAQSKKEKYEKIGEKKMNTSPEELCKGLPKE 240
                        250       260
                 ....*....|....*....|....*.
gi 392928060 247 FAQYLNYCRSLGFEEQPDYGYLRNLF 272
Cdd:cd14016  241 FAKYLEYVRSLKFEEEPDYDYLRQLF 266
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
8-272 5.34e-158

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271030  Cd Length: 266  Bit Score: 445.41  E-value: 5.34e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGP 87
Cdd:cd14128    1 KYRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  88 SLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRGNLVYIIDFGLAKRYRDSK-HQHIAY 166
Cdd:cd14128   81 SLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDSRtRQHIPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 167 RENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKAVTKRQKYELISEKKISTRVDDLCAGYPEA 246
Cdd:cd14128  161 REDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAE 240
                        250       260
                 ....*....|....*....|....*.
gi 392928060 247 FAQYLNYCRSLGFEEQPDYGYLRNLF 272
Cdd:cd14128  241 FAMYLNYCRGLRFEEAPDYMYLRQLF 266
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
9-289 6.42e-133

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028  Cd Length: 288  Bit Score: 382.54  E-value: 6.42e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   9 FRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGPS 88
Cdd:cd14126    2 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  89 LEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGL--GKRGNLVYIIDFGLAKRYRDSK-HQHIA 165
Cdd:cd14126   82 LEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRqsTKKQHVIHIIDFGLAKEYIDPEtNKHIP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 166 YRENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKAVTKRQKYELISEKKISTRVDDLCAGYPE 245
Cdd:cd14126  162 YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPE 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 392928060 246 AFAQYLNYCRSLGFEEQPDYGYLRNLFRTLFHRQQFCYDYVFDW 289
Cdd:cd14126  242 EMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDW 285
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
8-272 4.75e-131

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271029  Cd Length: 277  Bit Score: 377.60  E-value: 4.75e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGP 87
Cdd:cd14127    1 HYKVGKKIGEGSFGVIFEGTNLLNGQQVAIKFEPRKSDAPQLRDEYRTYKLLAGCPGIPNVYYFGQEGLHNILVIDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  88 SLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGL--GKRGNLVYIIDFGLAKRYRDSK-HQHI 164
Cdd:cd14127   81 SLEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRpgTKNANVIHVVDFGMAKQYRDPKtKQHI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 165 AYRENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKAVTKRQKYELISEKKISTRVDDLCAGYP 244
Cdd:cd14127  161 PYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQSTPIRDLCEGFP 240
                        250       260
                 ....*....|....*....|....*...
gi 392928060 245 EAFAQYLNYCRSLGFEEQPDYGYLRNLF 272
Cdd:cd14127  241 EEFAQYLEYVRNLGFDETPDYDYLRGLF 268
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
8-273 1.33e-73

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919  Cd Length: 263  Bit Score: 230.22  E-value: 1.33e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGP 87
Cdd:cd14017    1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  88 SLEDLF-NFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLG-KRGNLVYIIDFGLAKRYRDSKHQH-I 164
Cdd:cd14017   81 NLAELRrSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGpSDERTVYILDFGLARQYTNKDGEVeR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 165 AYRENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKavtkrqKYELISEKKISTRVDDLCAGYP 244
Cdd:cd14017  161 PPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLK------DKEEVGKMKEKIDHEELLKGLP 234
                        250       260
                 ....*....|....*....|....*....
gi 392928060 245 EAFAQYLNYCRSLGFEEQPDYGYLRNLFR 273
Cdd:cd14017  235 KEFFQILKHIRSLSYFDTPDYKKLHSLLE 263
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
5-272 2.58e-50

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917  Cd Length: 300  Bit Score: 170.92  E-value: 2.58e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   5 VGNRFRLGRKIGSGSFGDIYLGQNIQT-----NEEVAVKLEcVKSKHPqLHIESRLY-RIM-------------LGGIGI 65
Cdd:cd14015    8 TKRQWKLGKSIGQGGFGEIYLASDDSTlsvgkDAKYVVKIE-PHSNGP-LFVEMNFYqRVAkpemikkwmkakkLKHLGI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  66 PEIRWCG----QEGDYNVMVMELLGPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKR 141
Cdd:cd14015   86 PRYIGSGsheyKGEKYRFLVMPRFGRDLQKIFEKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLGFGKN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 142 GNLVYIIDFGLAKRYRDSKhQHIAYREN--KNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKAVT 219
Cdd:cd14015  166 KDQVYLVDYGLASRYCPNG-KHKEYKEDprKAHNGTIEFTSRDAHKGVAPSRRGDLEILGYNMLQWLCGKLPWEDNLKNP 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392928060 220 ---KRQKYELIseKKISTRVDDLCAG--YPEAFAQYLNYCRSLGFEEQPDYGYLRNLF 272
Cdd:cd14015  245 eyvQKQKEKYM--DDIPLLLKKCFPGkdVPEELQKYLKYVASLEYEEKPDYEKLRKIL 300
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
8-272 6.78e-40

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031  Cd Length: 262  Bit Score: 142.50  E-value: 6.78e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGP 87
Cdd:cd14129    1 RWKVLRKIGGGGFGEIYDALDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQLQGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  88 SLEDLFNFCQR-KFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMG-LGKRGNLVYIIDFGLAKRYRDSKHQHIA 165
Cdd:cd14129   81 NLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrFPSTCRKCYMLDFGLARQFTNSCGDVRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 166 YRENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKavtkrQKYELISekkISTRVDD--LCAGY 243
Cdd:cd14129  161 PRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIK-----DKEQVGS---IKERYEHrlMLKHL 232
                        250       260
                 ....*....|....*....|....*....
gi 392928060 244 PEAFAQYLNYCRSLGFEEQPDYGYLRNLF 272
Cdd:cd14129  233 PPEFSVFLDHISGLDYFTKPDYQLLVSVF 261
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
8-272 1.13e-39

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032  Cd Length: 262  Bit Score: 142.09  E-value: 1.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLGP 87
Cdd:cd14130    1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  88 SLEDLFNFCQR-KFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMG-LGKRGNLVYIIDFGLAKRYRDSKHQHIA 165
Cdd:cd14130   81 NLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrLPSTYRKCYMLDFGLARQYTNTTGEVRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 166 YRENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKavtKRQKYELISEkKISTRVddLCAGYPE 245
Cdd:cd14130  161 PRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIK---DKEQVGMIKE-KYEHRM--LLKHMPS 234
                        250       260
                 ....*....|....*....|....*..
gi 392928060 246 AFAQYLNYCRSLGFEEQPDYGYLRNLF 272
Cdd:cd14130  235 EFHLFLDHIASLDYFTKPDYQLIMSVF 261
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
6-269 8.04e-39

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK2 exists as two alternative splice forms, A and B, which differ in their C-terminal regions. VRK2A, the predominant isoform, contains a hydrophobic tail and is anchored to the ER and mitochondria. It is expressed in all cell types. VRK2B lacks a membrane-anchor tail and is detected in the cytosol and the nucleus. Like VRK1, it can stabilize p53. VRK2B functionally replaces VRK1 in the nucleus of cell types where VRK1 is absent. VRK2 modulates hypoxia-induced stress responses by interacting with TAK1, an atypical MAPK kinase kinase which triggers cascades that activate JNK following oxidative stress. VRK2 also interacts with JIP1, a scaffold protein that assembles three consecutive members of a MAPK pathway. This interaction prevents the association of JNK with the signaling complex, leading to reduced phosphorylation and AP1-dependent transcription. The VRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271025  Cd Length: 302  Bit Score: 140.75  E-value: 8.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   6 GNRFRLGRKIGSGSFGDIYLG--QNIQTNEEVAV---------------KLECVKSKHPQLHIESRLYRIMLGGIGIPeI 68
Cdd:cd14123   11 KKNWRLGKMIGKGGFGLIYLAspQVNVPVEDDAVhvikveyhengplfsELKFYQRAAKPDTISKWMKSKQLDYLGIP-T 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  69 RWCGQEGDYN-----VMVMELLGPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLgKRGN 143
Cdd:cd14123   90 YWGSGLTEFNgtsyrFMVMDRLGTDLQKILIDNGGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY-RNPN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 144 LVYIIDFGLAKRYRDSKhQHIAYREN--KNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPW-QGLKAVTK 220
Cdd:cd14123  169 EVYLADYGLSYRYCPNG-NHKEYKENprKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWeQNLKNPVA 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392928060 221 RQ--KYELISEKKISTRVDDLCAGYPEAFAQYLNYCRSLGFEEQPDYGYLR 269
Cdd:cd14123  248 VQeaKAKLLSNLPDSVLKWSTGGSSSMEIAQFLSRVKDLAYDEKPDYQALK 298
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
9-284 6.30e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 131.79  E-value: 6.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   9 FRLGRKIGSGSFGDIYLGQNIQTN--EEVAVKLECVKSKHPQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELL- 85
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDRKLValKVLAKKLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVMEYVd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  86 GPSLEDLF--NFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNLVYIIDFGLAKRYRDSKHQH 163
Cdd:COG0515   82 GGSLEDLLkkIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIL--LDRDGRVVKLIDFGLAKLLPDPGSTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 164 IAYRENKNLTGTARYASINTHRGIEQ---SRRDDIESLGYVFMYFNRGTLPWQGLKAV-----TKRQKYELISEKKISTR 235
Cdd:COG0515  160 SIPALPSTSVGTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSsatsqTLKIILELPTPSLASPL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 392928060 236 VDDLCAGYPEAFAQYLNycRSLGFEEQPDYGYLRNLFRTLFHRQQFCYD 284
Cdd:COG0515  240 SPSNPELISKAASDLLK--KLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
STKc_VRK1 cd14122
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs ...
8-272 7.31e-33

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. Vertebrates contain three VRK proteins. Human VRK1 is implicated in the regulation of many cellular processes including cell cycle progression and proliferation, stress responses, nuclear envelope assembly and chromatin condensation. It regulates cell cycle progression during the DNA replication period by inducing cyclin D1 expression. VRK1 also phosphorylates and regulates some transcription factors including p53, c-Jun, ATF2, and nuclear factor BAF. VRK1 stabilizes p53 by interfering with its mdm2-mediated degradation. Accumulation of p53, which blocks cell growth and division, is modulated by an autoregulatory loop between p53 and VRK1 (accumulated p53 downregulates VRK1). This autoregulatory loop has been found to be nonfunctional in some lung carcinomas. The VRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271024  Cd Length: 301  Bit Score: 124.61  E-value: 7.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGqNIQTNEEVAVKLECVKSKHPQ----LHIESRLYRIM--------------LGGIGIPEIR 69
Cdd:cd14122   11 EWKLGLPIGQGGFGRLYLA-DENSSESVGSDAPYVVKVEPSdngpLFTELKFYMRAakpdqiqkwikshkLKYLGVPKYW 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  70 WCG---QEGD-YNVMVMELLGPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLgKRGNLV 145
Cdd:cd14122   90 GSGlheKNGKsYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLGLRILDILEYIHEHEYVHGDIKASNLLLSY-KNPDQV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 146 YIIDFGLAKRY-RDSKHQHIAYRENKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQglkavTKRQKY 224
Cdd:cd14122  169 YLVDYGLAYRYcPEGVHKEYKEDPKRCHDGTIEFTSIDAHKGVAPSRRGDLEILGYCMIQWLCGHLPWE-----DNLKDP 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392928060 225 ELISEKKISTRVD-----DLC---AGYPEAFAQYLNYCRSLGFEEQPDYGYLRNLF 272
Cdd:cd14122  244 NYVRDSKIRYRDNiselmEKCfpgKNKPGEIRKYMETVKLLGYTEKPLYPHLREIL 299
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
15-206 2.24e-32

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622  Cd Length: 215  Bit Score: 121.22  E-value: 2.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  15 IGSGSFGDIYLGQNIQTNEEVAVKLECVKSKHPQLHIESRLYRIM--LGGIGIPEIRWCGQEGDYNVMVMELL-GPSLED 91
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILkkLNHPNIVKLYDVFETENFLYLVMEYCeGGSLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  92 LFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMglgKRGNLVYIIDFGLAKRYRDSKHQhiayRENKN 171
Cdd:cd00180   81 LLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL---DSDGTVKLADFGLAKDLDSDDSL----LKTTG 153
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392928060 172 LTGTARYASINTHRGIEQSRRDDIESLGYVFMYFN 206
Cdd:cd00180  154 GTTPPYYAPPELLGGRYYGPKVDIWSLGVILYELE 188
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
9-239 3.78e-27

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567  Cd Length: 254  Bit Score: 107.62  E-value: 3.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060     9 FRLGRKIGSGSFGDIYLGQNIQTNEEVAVK---LECVKSKHPQLHIESRLYRiMLGGIGIPEIRWCGQEGDYNVMVMELL 85
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILK-KLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060    86 -GPSLEDLFNFcQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNlVYIIDFGLAKRYRDSKHQHi 164
Cdd:smart00220  80 eGGDLFDLLKK-RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL--LDEDGH-VKLADFGLARQLDPGEKLT- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   165 ayrenkNLTGTARYASINTHRGIEQSRRDDIESLGyVFMY-FNRGTLPWQG-------LKAVTKRQKYELISEKKISTRV 236
Cdd:smart00220 155 ------TFVGTPEYMAPEVLLGKGYGKAVDIWSLG-VILYeLLTGKPPFPGddqllelFKKIGKPKPPFPPPEWDISPEA 227

                   ...
gi 392928060   237 DDL 239
Cdd:smart00220 228 KDL 230
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
8-214 5.19e-27

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916  Cd Length: 260  Bit Score: 107.29  E-value: 5.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLecvkskhpqLHIE--------SRLYR---IM--LGGIGIPEIRWCGQE 74
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKV---------LRPElaedeefrERFLRearALarLSHPNIVRVYDVGED 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  75 GDYNVMVMELL-GPSLEDLFNFcQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNlVYIIDFGLA 153
Cdd:cd14014   72 DGRPYIVMEYVeGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANIL--LTEDGR-VKLTDFGIA 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392928060 154 KRYRDSKHQHiayreNKNLTGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQG 214
Cdd:cd14014  148 RALGDSGLTQ-----TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDG 203
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
63-270 1.71e-26

Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271026  Cd Length: 298  Bit Score: 106.47  E-value: 1.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  63 IGIPEIRWCGQEGDYNVMVMELLGPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRG 142
Cdd:cd14124   82 LGIPSCVGFGVHDSYRFLVFPSLGQSLQSALDEGKGVLSEKAVLQLACRLLDALEFIHENEYVHGDITAENIFVDPEDQS 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 143 NlVYIIDFGLAKRYRDSKhQHIAYRENKNLT--GTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKAVTK 220
Cdd:cd14124  162 E-VYLAGYGFAFRYCPGG-KHVEYREGSRSPheGDIEFISLDSHKGAGPSRRSDLQSLGYCMLKWLTGSLPWSNLLHNTE 239
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392928060 221 RQKYElisEKKISTRVDDL---CAGY---PEAFAQYLNYCRSLGFEEQPDYGYLRN 270
Cdd:cd14124  240 DIMKQ---KERFMDDVPGFlgpCFHQkkvSEALQKYLKVVMALQYEEKPDYAMLRN 292
Pkinase pfam00069
Protein kinase domain;
9-214 2.47e-22

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 93.82  E-value: 2.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060    9 FRLGRKIGSGSFGDIYLGQNIQTNEEVAVKleCVKSKHPQLHIESRLYR---IM--LGGIGIPEIRWCGQEGDYNVMVME 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIK--KIKKEKIKKKKDKNILReikILkkLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   84 LL-GPSLEDLFNFcQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNLvYIIDFGLAKRYRDSKhq 162
Cdd:pfam00069  79 YVeGGSLFDLLSE-KGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENIL--IDEDGNL-KITDFGLARQLNSGS-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392928060  163 hiayrENKNLTGTARYAS--INTHRGIeqSRRDDIESLGYVFMYFNRGTLPWQG 214
Cdd:pfam00069 153 -----SLTSFVGTPWYMApeVLRGNPY--GPKVDVWSLGCILYELLTGKPPFPG 199
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
6-272 1.27e-21

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 92.32  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   6 GNRFRLGRKIGSGSFGDIYLGQ---NIQTNEEVAVKLECVKSKhpQLHIESRLYRIM--------------LGGIGIPEI 68
Cdd:PHA02882  11 GKEWKIDKLIGCGGFGCVYETQcasDHCINNQAVAKIENLENE--TIVMETLVYNNIydidkialwknihnIDHLGIPKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  69 RWCGQ----EGDYNVMVMELLGPSLEDLFN--FCQRKFSLKTVLLladQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRG 142
Cdd:PHA02882  89 YGCGSfkrcRMYYRFILLEKLVENTKEIFKriKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMVDGNNRG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 143 nlvYIIDFGLAKrYRDSKHQHIAY-RENKNL-TGTARYASINTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQGLKA--- 217
Cdd:PHA02882 166 ---YIIDYGIAS-HFIIHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHngn 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392928060 218 ---VTKRQKYELISEKKISTRVDDlcagypEAFAQYLNYCRSLGFEEQPDYGYLRNLF 272
Cdd:PHA02882 242 lihAAKCDFIKRLHEGKIKIKNAN------KFIYDFIECVTKLSYEEKPDYDALIKIF 293
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
8-199 9.03e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783  Cd Length: 258  Bit Score: 89.50  E-value: 9.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVK-LECVKSKHP---QLHIESRLYRIMlggiGIPEI---RWCGQEGDYNVM 80
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKeVELSGDSEEeleALEREIRILSSL----KHPNIvryLGTERTENTLNI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  81 VMELL-GPSLEDLF-NFcqRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRgnlVYIIDFGLAKRYRD 158
Cdd:cd06606   77 FLEYVpGGSLASLLkKF--GKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGV---VKLADFGCAKRLAE 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392928060 159 SKHQHiayrENKNLTGTARYASINTHRGIEQSRRDDIESLG 199
Cdd:cd06606  152 IATGE----GTKSLRGTPYWMAPEVIRGEGYGRAADIWSLG 188
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
8-212 1.58e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796  Cd Length: 265  Bit Score: 88.90  E-value: 1.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLecVKSKHPQLHIESRLYRIM--LGGIGIPEI-RWCGQEGDYNVMV--M 82
Cdd:cd06626    1 RWQRGNKIGEGTFGKVYTAVNLDTGELMAMKE--IRFQDNDPKTIKEIADEMkvLEGLDHPNLvRYYGVEVHREEVYifM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  83 ELL-GPSLEDLFNF-------CQRKFSLktvllladQMLSRVEFIHCRDYIHRDIKPDNFLMGlgkRGNLVYIIDFGLAK 154
Cdd:cd06626   79 EYCqEGTLEELLRHgrildeaVIRVYTL--------QLLEGLAYLHENGIVHRDIKPANIFLD---SNGLIKLGDFGSAV 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392928060 155 RYRDSKhQHIAYRENKNLTGTARYAS---INTHRGIEQSRRDDIESLGYVFMYFNRGTLPW 212
Cdd:cd06626  148 KLKNNT-TTMAPGEVNSLVGTPAYMApevITGNKGEGHGRAADIWSLGCVVLEMATGKRPW 207
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
8-233 1.97e-20

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905  Cd Length: 252  Bit Score: 88.34  E-value: 1.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVK------------------LECVKS-KHPqlHIeSRLYRIMlggigipei 68
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKiidksklkeeieekikreIEIMKLlNHP--NI-IKLYEVI--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  69 rwcgQEGDYNVMVMELLgpSLEDLFNF-CQR-KFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNLVy 146
Cdd:cd14003   69 ----ETENKIYLVMEYA--SGGELFDYiVNNgRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENIL--LDKNGNLK- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 147 IIDFGLAKRYRDSKHQHIAYrenknltGTARYAS--INTHRGiEQSRRDDIESLG---YVFMYfnrGTLPWQGlkaVTKR 221
Cdd:cd14003  140 IIDFGLSNEFRGGSLLKTFC-------GTPAYAApeVLLGRK-YDGPKADVWSLGvilYAMLT---GYLPFDD---DNDS 205
                        250
                 ....*....|..
gi 392928060 222 QKYELISEKKIS 233
Cdd:cd14003  206 KLFRKILKGKYP 217
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
13-163 2.23e-20

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688  Cd Length: 249  Bit Score: 88.06  E-value: 2.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  13 RKIGSGSFGDIYLGQNIQTNEEVAVK-LECVKSKHPQLHIESRLYRIMLGGIGIP-------EIRWcgQEGDYNVMVMEL 84
Cdd:cd05118    5 RKIGEGAFGTVWLARDKVTGEKVAIKkIKNDFRHPKAALREIKLLKHLNDVEGHPnivklldVFEH--RGGNHLCLVFEL 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392928060  85 LGPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRgnLVYIIDFGLAKRYRDSKHQH 163
Cdd:cd05118   83 MGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELG--QLKLADFGLARSFTSPPYTP 159
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
8-163 4.24e-20

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687  Cd Length: 258  Bit Score: 87.15  E-value: 4.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVK-----------LECVKS--------KHPqlHIeSRLYRIMlggigipei 68
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKiidkkklksedEEMLRReieilkrlDHP--NI-VKLYEVF--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  69 rwcgQEGDYNVMVMELL--GpsleDLFNF-CQR-KFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRGNL 144
Cdd:cd05117   69 ----EDDKNLYLVMELCtgG----ELFDRiVKKgSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSP 140
                        170
                 ....*....|....*....
gi 392928060 145 VYIIDFGLAKRYRDSKHQH 163
Cdd:cd05117  141 IKIIDFGLAKIFEEGEKLK 159
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
9-199 7.76e-20

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692  Cd Length: 254  Bit Score: 86.49  E-value: 7.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   9 FRLGRKIGSGSFGDIYLGQNIQTNEEVAVKlecvkskhpQLHIESRLYRIMLggigIPEIRW--------------CGQE 74
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIK---------KINLESKEKKESI----LNEIAIlkkckhpnivkyygSYLK 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  75 GDYNVMVMELL-GPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGL-GKrgnlVYIIDFGL 152
Cdd:cd05122   69 KDELWIVMEFCsGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSdGE----VKLIDFGL 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 392928060 153 AKRYRDSKhqhiayrENKNLTGTARYASINTHRGIEQSRRDDIESLG 199
Cdd:cd05122  145 SAQLSDGK-------TRNTFVGTPYWMAPEVIQGKPYGFKADIWSLG 184
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
9-154 6.40e-17

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823  Cd Length: 282  Bit Score: 78.29  E-value: 6.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   9 FRLGRKIGSGSFGDIYLGQNIQTNEEVAVKL-------ECVKS------------KHPqlHIeSRLYRIMLGGIGIpeir 69
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKirldneeEGIPStalreisllkelKHP--NI-VKLLDVIHTENKL---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  70 wcgqegdynVMVMELLGPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGlgkRGNLVYIID 149
Cdd:cd07829   74 ---------YLVFEYCDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLIN---RDGVLKLAD 141

                 ....*
gi 392928060 150 FGLAK 154
Cdd:cd07829  142 FGLAR 146
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
7-180 9.95e-17

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733  Cd Length: 278  Bit Score: 78.03  E-value: 9.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   7 NRFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLeCVKS------KHPQLHIEsRLYRIMLGGIGIPEIRWCGQEGDYNVM 80
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKV-LDKRhiikekKVKYVTIE-KEVLSRLAHPGIVKLYYTFQDESKLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  81 VMELL--GpsleDLFNFCQRK--FSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRgnlVYIIDFGLAKRY 156
Cdd:cd05581   79 VLEYApnG----DLLEYIRKYgsLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH---IKITDFGTAKVL 151
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392928060 157 RDSK-----------HQHIAYRENKNLTGTARYAS 180
Cdd:cd05581  152 GPDSspestkgdadsQIAYNQARAASFVGTAEYVS 186
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
9-160 1.14e-16

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824  Cd Length: 283  Bit Score: 77.57  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   9 FRLGRKIGSGSFGDIYLGQNIQTNEEVAVKL---------EC-----VKS-----KHPqlHIEsRLYRImlggigipeIR 69
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKmkkkfysweECmnlreVKSlrklnEHP--NIV-KLKEV---------FR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  70 wcgqEGDYNVMVMELLGPSLEDLF-NFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMglgKRGNLVYII 148
Cdd:cd07830   69 ----ENDELYFVFEYMEGNLYQLMkDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV---SGPEVVKIA 141
                        170
                 ....*....|..
gi 392928060 149 DFGLAKRYRDSK 160
Cdd:cd07830  142 DFGLAREIRSRP 153
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
11-178 4.51e-16

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826  Cd Length: 287  Bit Score: 76.21  E-value: 4.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  11 LGRkIGSGSFGDIYLGQNIQTNEEVAVKLECVKSKH----PQLHIESRLYRIMLGGIGIPEIRWCGQEGDYNVMVMELLG 86
Cdd:cd07832    5 LGR-IGEGAHGIVFKAKDRETGETVALKKVALRKLEggipNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYML 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  87 PSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNLvYIIDFGLAKRY-----RDSKH 161
Cdd:cd07832   84 SSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLL--ISSTGVL-KIADFGLARLFseedpRLYSH 160
                        170       180
                 ....*....|....*....|
gi 392928060 162 QhIA---YRENKNLTGTARY 178
Cdd:cd07832  161 Q-VAtrwYRAPELLYGSRKY 179
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
9-212 1.21e-15

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971  Cd Length: 261  Bit Score: 74.67  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   9 FRLGRKIGSGSFGDIYLGQNIQTNEEVAVKLECVKsKHPQLHIES--RLYRI--MLGGIGIPEIRWCGQEGDYNVMVMEL 84
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMK-RAPGDCPENikKEVCIqkMLSHKNVVRFYGHRREGEFQYLFLEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  85 LgpSLEDLF-----------NFCQRKFSlktvllladQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNLvYIIDFGLA 153
Cdd:cd14069   82 A--SGGELFdkiepdvgmpeDVAQFYFQ---------QLMAGLKYLHSCGITHRDIKPENLL--LDENDNL-KISDFGLA 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392928060 154 KRYR-DSKHqhiayRENKNLTGTARYA-----SINTHRGieqsRRDDIESLGYVFMYFNRGTLPW 212
Cdd:cd14069  148 TVFRyKGKE-----RLLNKMCGTLPYVapellAKKKYRA----EPVDVWSCGIVLFAMLAGELPW 203
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
13-239 3.35e-15

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986  Cd Length: 275  Bit Score: 73.58  E-value: 3.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  13 RKIGSGSFGDIYLGQNIQTNEEVAVK-LECVKSKHPQLHIESRLYRIM--------LGGIGIPEIRWCGQEGDYNVMVME 83
Cdd:cd14084   12 RTLGSGACGEVKLAYDKSTCKKVAIKiINKRKFTIGSRREINKPRNIEteieilkkLSHPCIIKIEDFFDAEDDYYIVLE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  84 LLGPSleDLFNFCQRKFSLK--TVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGLGKRGNLVYIIDFGLAKRYRDSKH 161
Cdd:cd14084   92 LMEGG--ELFDRVVSNKRLKeaICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFGLSKILGETSL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 162 QhiayrenKNLTGTARYAS---INTHRGIEQSRRDDIESLGYVFMYFNRGTLPWQG------LKAVTKRQKYELISE--K 230
Cdd:cd14084  170 M-------KTLCGTPTYLApevLRSFGTEGYTRAVDCWSLGVILFICLSGYPPFSEeytqmsLKEQILSGKYTFIPKawK 242

                 ....*....
gi 392928060 231 KISTRVDDL 239
Cdd:cd14084  243 NVSEEAKDL 251
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
15-233 1.24e-14

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910  Cd Length: 267  Bit Score: 71.82  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  15 IGSGSFGDIYLGQNIQTNEEVAVKlECVKSK--------------------------------HPqlHIeSRLYRImlgg 62
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIK-IFNKSRlrkrregkndrgkiknalddvrreiaimkkldHP--NI-VRLYEV---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  63 IGIPEirwcgqeGDYNVMVMELL--GPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGlgk 140
Cdd:cd14008   73 IDDPE-------SDKLYLVLEYCegGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLT--- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060 141 RGNLVYIIDFGLAkryrdskhqHIAYRENKNLTGTA-RYA-----SINTHRGIEQSRRDDIESLG---YVFMYfnrGTLP 211
Cdd:cd14008  143 ADGTVKISDFGVS---------EMFEDGNDTLQKTAgTPAflapeLCDGDSKTYSGKAADIWALGvtlYCLVF---GRLP 210
                        250       260
                 ....*....|....*....|....*..
gi 392928060 212 WQG-----LKAVTKRQKYELISEKKIS 233
Cdd:cd14008  211 FNGdnileLYEAIQNQNDEFPIPPELS 237
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
8-153 2.20e-14

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895  Cd Length: 267  Bit Score: 71.23  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   8 RFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKleCVK------------SKHPQLHiESRLYRIMLGGIGIPEIRWCGQEG 75
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIK--CLYksgpnskdgndfQKLPQLR-EIDLHRRVSRHPNIITLHDVFETE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  76 DYNVMVMELLgpSLEDLFNFC--QRKFSLKTVLL--LADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNLVYIIDFG 151
Cdd:cd13993   78 VAIYIVLEYC--PNGDLFEAIteNRIYVGKTELIknVFLQLIDAVKHCHSLGIYHRDIKPENIL--LSQDEGTVKLCDFG 153

                 ..
gi 392928060 152 LA 153
Cdd:cd13993  154 LA 155
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
15-155 2.42e-14

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693  Cd Length: 250  Bit Score: 70.62  E-value: 2.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  15 IGSGSFGDIYLGQNIQTNEEVAVKL----ECVKSKHpQLHIESRlyRIMLGGIGIPEI---RWCGQEGDYNVMVMELL-- 85
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVlrkkEIIKRKE-VEHTLNE--RNILERVNHPFIvklHYAFQTEEKLYLVLDYVpg 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392928060  86 GpsleDLFNFCQR--KFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNLVyIIDFGLAKR 155
Cdd:cd05123   78 G----ELFSHLSKegRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENIL--LDSDGHIK-LTDFGLAKE 142
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
14-153 3.03e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789  Cd Length: 255  Bit Score: 70.70  E-value: 3.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  14 KIGSGSFGDIYLGQNIQTNEEVAVKlecvkskhpQLHIESRLYRIMLGGIGIpeIRWCGQE-----------GDYNVMVM 82
Cdd:cd06614    7 KIGEGASGEVYKATDRATGKEVAIK---------KMRLRKQNKELIINEILI--MKECKHPnivdyydsylvGDELWVVM 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392928060  83 ELL-GPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLGKRGNlVYIIDFGLA 153
Cdd:cd06614   76 EYMdGGSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNIL--LSKDGS-VKLADFGFA 144
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
10-154 3.10e-14

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581  Cd Length: 257  Bit Score: 70.64  E-value: 3.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060    10 RLGRKIGSGSFGDIYLGQNIQTN----EEVAVKleCVKSKHPQLHIESrLYR---IM----------LGGIgipeirwCG 72
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGgkkkVEVAVK--TLKEDASEQQIEE-FLRearIMrkldhpnvvkLLGV-------CT 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060    73 QEGDYnVMVMELL-GPSLEDLFNFCQRKFSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLMGlgkRGNLVYIIDFG 151
Cdd:smart00219  72 EEEPL-YIVMEYMeGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG---ENLVVKISDFG 147

                   ...
gi 392928060   152 LAK 154
Cdd:smart00219 148 LSR 150
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
7-160 3.58e-14

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725  Cd Length: 350  Bit Score: 71.55  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060   7 NRFRLGRKIGSGSFGDIYLGQNIQTNEEVAVKL----ECVKSKHPQLHIESRLyrIMLGGIG--IPEIRWCGQEGDYNVM 80
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKIlrksDMLKREQIAHVRAERD--ILADADSpwIVRLHYAFQDEDHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928060  81 VMELLGPSleDLFNFCQRK--FSLKTVLLLADQMLSRVEFIHCRDYIHRDIKPDNFLmgLG